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Database: UniProt
Entry: D1VZ52_9BACT
LinkDB: D1VZ52_9BACT
Original site: D1VZ52_9BACT 
ID   D1VZ52_9BACT            Unreviewed;       659 AA.
AC   D1VZ52;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   SubName: Full=Succinate dehydrogenase flavoprotein subunit {ECO:0000313|EMBL:EFA97731.1};
DE            EC=1.3.5.1 {ECO:0000313|EMBL:EFA97731.1};
GN   Name=sdhA {ECO:0000313|EMBL:EFA97731.1};
GN   ORFNames=HMPREF9019_1497 {ECO:0000313|EMBL:EFA97731.1};
OS   Hoylesella timonensis CRIS 5C-B1.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Hoylesella.
OX   NCBI_TaxID=679189 {ECO:0000313|EMBL:EFA97731.1, ECO:0000313|Proteomes:UP000004001};
RN   [1] {ECO:0000313|EMBL:EFA97731.1, ECO:0000313|Proteomes:UP000004001}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CRIS 5C-B1 {ECO:0000313|EMBL:EFA97731.1,
RC   ECO:0000313|Proteomes:UP000004001};
RA   Durkin A.S., Madupu R., Torralba M., Methe B., Sutton G., Strausberg R.L.,
RA   Nelson K.E.;
RT   "Genome Sequence of Prevotella timonensis CRIS 5C-B1.";
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EFA97731.1}.
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DR   EMBL; ADEF01000028; EFA97731.1; -; Genomic_DNA.
DR   AlphaFoldDB; D1VZ52; -.
DR   eggNOG; COG1053; Bacteria.
DR   Proteomes; UP000004001; Unassembled WGS sequence.
DR   GO; GO:0102040; F:fumarate reductase (menaquinone); IEA:UniProtKB-EC.
DR   GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 1.20.58.100; Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal domain; 1.
DR   Gene3D; 3.90.700.10; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR   InterPro; IPR003953; FAD-binding_2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR037099; Fum_R/Succ_DH_flav-like_C_sf.
DR   InterPro; IPR015939; Fum_Rdtase/Succ_DH_flav-like_C.
DR   InterPro; IPR030664; SdhA/FrdA/AprA.
DR   InterPro; IPR011280; Succ_DH/Fum_Rdt_flav_su.
DR   InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR   NCBIfam; TIGR01811; sdhA_Bsu; 1.
DR   PANTHER; PTHR11632; SUCCINATE DEHYDROGENASE 2 FLAVOPROTEIN SUBUNIT; 1.
DR   PANTHER; PTHR11632:SF53; SUCCINATE DEHYDROGENASE FLAVOPROTEIN SUBUNIT; 1.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   Pfam; PF02910; Succ_DH_flav_C; 1.
DR   PRINTS; PR00368; FADPNR.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF46977; Succinate dehydrogenase/fumarate reductase flavoprotein C-terminal domain; 1.
DR   SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
PE   4: Predicted;
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:EFA97731.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004001}.
FT   DOMAIN          36..460
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          522..657
FT                   /note="Fumarate reductase/succinate dehydrogenase
FT                   flavoprotein-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02910"
FT   ACT_SITE        338
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630664-50"
SQ   SEQUENCE   659 AA;  73768 MW;  C2B073F5DC3ED67D CRC64;
     MTQIDSKIPE GPVAEKWTNY KAHQRLVNPK NKLKLDVIVV GTGLAGASAA ASLGEMGFNV
     FNFCIQDSPR RAHSIAAQGG INAAKDYQND GDSVYRLFYD TVKGGDYRAR EANVYRLAEV
     SNAIIDQCVA QGVPFAREYG GMLANRSFGG AQVSRTFYAK GQTGQQLLLG AYSSLMCQVH
     AGKVKLYTRY EMEDVVIIDG RARGIIAKNL VTGKLERFSA NAVVIATGGY GNAYFLSTNA
     MGCNCTAAVQ CYRKGAYFAN PSYVQIHPTC IPVHGDKQSK LTLMSESLRN DGRIWVPKKI
     EDAKALQAGT KQGWEIPEED RDYYLERRYP AFGNLVPRDV ASRAAKERCD KGFGVNNTGL
     AVFLDFSESI NRLGLDEIMQ RYGNLFEMYE EITDVFPGDM ANEINGVKYY KPMMIFPAIH
     YTMGGIWVDY ELMTSVTGLF AIGECNFSDH GANRLGASAL MQGLADGYFV LPYTIQNYLA
     DQAVWPRLSI DLPEFEEAEK KVQSEIDRLM NIKGKRSVDS IHKELGHIMW EHVGMGRTKE
     GLEEGLKMIA DLRKEFDTNL FIPGTKEGLN VELDKAIHLR DFLLMGELVA YDAISRNESC
     GGHFREEYQT PEGEAKRDDE NYFYVGCWKY QNNDETAPEL IKEPLEYEAI KVQTRNYKN
//
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